HmoB

• Description: heme monooxygenase
  
  

Gene name	hmoB
Synonyms	yixC, yhgC
Essential	no
Product	heme monooxygenase
Function	degradation of heme, acquisition of iron
Gene expression levels in SubtiExpress: hmoB
MW, pI	18 kDa, 5.216
Gene length, protein length	498 bp, 166 aa
Immediate neighbours	yhgB, pbpF
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

acquisition of iron

The gene

Basic information

• Locus tag: BSU10100

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: binds hemin in vitro with ~1:1 stoichiometry and degrade hemin in the presence of an electron donor PubMed

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure: 3TVZ PubMed

• UniProt: P38049

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: hmoB PubMed

• Expression browser: hmoB PubMed

• Sigma factor:

• Regulation:
  • constitutively expressed PubMed

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Additional references: PubMed

Seonghun Park, Sarah Choi, Jungwoo Choe
Bacillus subtilis HmoB is a heme oxygenase with a novel structure.
BMB Rep: 2012, 45(4);239-41
[PubMed:22531134] [WorldCat.org] [DOI] (I p)

D L Popham, P Setlow
Cloning, nucleotide sequence, and regulation of the Bacillus subtilis pbpF gene, which codes for a putative class A high-molecular-weight penicillin-binding protein.
J Bacteriol: 1993, 175(15);4870-6
[PubMed:8335642] [WorldCat.org] [DOI] (P p)